Research on cell interactions with extracellular matrix has exploded over the past 10 years. Fibronectin has been the prototype extracellular matrix molecule for this Gordon Conference, which started in 1982. The discovery of integrins in the mid 1980's, as receptors for fibronectin and other constituents of the extracellular matrix expanded the scope of the conference. Together, fibronectin and integrins control many basic biologic processes, including cell adhesion, determination of cell shape, organization of the cytoskeleton and the extracellular matrix, regulation of morphogenesis and tissue interactions, immune cell trafficking, and hemostasis. Important insights have developed over the past 2-4 years, as follows. The activation state of integrins is tightly regulated, and is critical in determining their ability to bind ligand and to transduce signals. Signaling complexes assembled at adhesion sites bring together cytoskeletal components, nonreceptor tyrosine kinases, and other mediators of signal transduction. Integrin ligation activates similar downstream signaling pathways as receptors for growth factors. In fact neither integrins nor growth factor receptors may be able signal effectively in isolation. Along these lines, single extracellular matrix components, including fibronectin and collagen, have recently been reported to bind directly, and/or activate, receptor tyrosine kinases as well as integrins. Finally, new families of ligands: the disintegrins, and the emergence of other classes of integrin-associated proteins: the TM-4 proteins, have further broadened the context within which integrins function. The conference outlined in this application is directed at communicating these exciting new developments and at stimulating discussion among participants from different disciplines. This cross pollination is a most effective way of stimulating yet new waves of insight and information.